ID S6BM25_PSERE Unreviewed; 878 AA.
AC S6BM25;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN ECO:0000313|EMBL:BAN50304.1};
GN ORFNames=PCA10_45720 {ECO:0000313|EMBL:BAN50304.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50304.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN50304.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50304.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00595};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP013068; BAN50304.1; -; Genomic_DNA.
DR RefSeq; WP_016494433.1; NC_021499.1.
DR AlphaFoldDB; S6BM25; -.
DR STRING; 1245471.PCA10_45720; -.
DR KEGG; pre:PCA10_45720; -.
DR PATRIC; fig|1245471.3.peg.4624; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000015503; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW Pyruvate {ECO:0000313|EMBL:BAN50304.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 545
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 878 AA; 97019 MW; 9B2CD778F0B9C1B5 CRC64;
MAEIDARLRE DVHLLGELLG DTIRAQLGEA FLDKIERIRK GAKAARQGSA QGERQLNETL
DGLSDDELLP VARAFNQFLN LANIAEQYHR IRRRGPDEPQ PFEDRVLDNL LQRLLAAGHG
PEQLARQLGR LEIELVLTAH PTEVARRTLI QKYDAMAAQL AAQDHADLSA AERDAVRLRL
LRLIAEAWHT EEIRRIRPTP LDEAKWGFAV IEHSLWQALP NVLRHVDQAL HAATGLRLPL
TAAPLRFASW MGGDRDGNPN VTAAISRQVL LLARWMAADL YLRDVDHLAA ELSMQQASDE
LRVRVGVHPE PYRALLKQLR DRLRATRTWA ESALDADVPP CAEVLHDNTQ LLEPLELCYH
SLHACGMGVI ADGALLDCLR RAATFGLFLV RLDIRQDSAR HAAALDEITD YLGLGNYAQW
SEEQRLTFLQ RELDNRRPLL PPHYRPSADT AEVLATCKVV ANAPAASLGS YVISMAGAPS
DVLAVQLLLK EAGLQRPIHV VPLFETLADL DNAAPAIDRL LGLPGYRARL HGPQEVMIGY
SDSAKDAGTV AAAWAQYRAQ EQLVEVCRAH QVELLLFHGR GGTVGRGGGP AHAAILSQPP
GSVAGRFRTT EQGEMIRFKF GLPGIAEQNL NTYLAAVLEA TLMPPPEPEP AWRAAMDRLA
ADGVAAYRAV VREHPQFVDY FRQATPEQEL GRLPLGSRPA KRRAGGVESL RAIPWIFAWT
QTRLMLPAWL GWEAALANAT QRGETRLLAR MREHWPFFAT RIDMLEMVLA KADANIAALY
DERLVPEELE PLGVQLRDLL SQACASVLAL TGQSELLAAS PETREAISVR NTYLDPLHLL
QTELLARSRR SEQHVEGPLE QALLVSVAGI AAGLRNTG
//